Methyl-accepting chemotaxis protein
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| Methyl-accepting chemotaxis protein with Fe-protoporphyrin IX + O2 1xbn | |||||||||
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| Ligands: | , | ||||||||
| Gene: | Tar4 (Thermoanaerobacter tengcongensis MB4) | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Methyl-accepting chemotaxis protein (MCP) are proteins of the inner cytoplasmic face of bacterial plasma membrane with which the receptors of the outer face interact. MCP undergo reversible methylation as part of the adaptation to the signal. MCP which are NO sensing contain a heme-NO and oxygen-binding domain (H-NOX). The images at the left and at the right correspond to one representative MCP, i.e. the crystal structure of Methyl-accepting chemotaxis protein from Thermoanaerobacter tengcongensis (3hbt).
3D Structures of Methyl-accepting chemotaxis protein3D Structures of Methyl-accepting chemotaxis protein
3g67 – TmMCP – Thermotoga maritima 3g6b - TmMCP (mutant) 2ch7 – TmMCP cytoplasmic domain 3c8c - MCP N terminal – Vibrio cholerae 2qhx - MCP N terminal – Vibrio parahaemolyticus 2d4u – EcMCP ligand-binding domain (mutant) – Eschericia coli 1qu7 - EcMCP I cytoplasmic domain 1jmw - MCP II ligand-binding domain (mutant) – Salmonella typhimurium
Heme-containing MCP
3sj5 – MCP (mutant) with Fe-protoporphyrin IX – Caldanaerobacter subterraneus 3nvr, 3nvu, 3iqb, 3eee – TtMCP N terminal (mutant) with Fe-protoporphyrin IX + O2 – Thermoanaerobacter tengcongensis 1xbn - TtMCP with Fe-protoporphyrin IX + O2 1u4h, 1u55, 1u56 - TtMCP H-NOX domain with Fe-protoporphyrin IX + O2 3lah, 3lai - TtMCP N terminal (mutant) with Fe-protoporphyrin IX + imidazole 3m0b - TtMCP N terminal with Ru-mesoporphyrin IX